What are MMP substrates?
The matrix metalloproteinases (MMP) are a family of peptidase enzymes responsible for the degradation of extracellular matrix components, including collagen, gelatin, Fibronectin, Laminin and proteoglycan. Biochemicals that act as substrates for MMP have many applications in biochemical and physiological research.
What do MMPs cleave?
MMPs may be described as multifunctional enzymes capable of cleaving the extracellular matrix components (collagens, laminin, fibronectin, vitronectin, aggrecan, enactin, versican, perlecan, tenascin, elastin and many others), growth factors, cytokines and cell surface-associated adhesion and signaling receptors.
What does MMP 7 do?
MMP-7 plays a role in remodeling of tissues involved in development and reproduction such as the uterus, and could play a role in remodeling following tissue injury. MMP-7 degrades ECM components and cleaves cell-surface molecules such as Fas–ligand, pro-TNF-α, syndecan-1, and E-cadherin to generate soluble forms.
What does MMP degrade?
The collagenases are capable of degrading triple-helical fibrillar collagens into distinctive 3/4 and 1/4 fragments. These collagens are the major components of bone, cartilage and dentin, and MMPs are the only known mammalian enzymes capable of degrading them.
What produces MMP?
MMPs are produced by many cell types, including lymphocytes and granulocytes, but in particular by activated macrophages (17). Their generation of chemotactic fragments from ECM proteins may also contribute to the recruitment of inflammatory cells (22, 40).
Where is MMP found?
Abstract. Matrix metalloproteinases (MMPs), also called matrixins, function in the extracellular environment of cells and degrade both matrix and non-matrix proteins.
What are the substrate specificities of MMP-2?
The peptide substrate sequence specificities of human MMP-2 ( Chapter 156) and MMP-9 are similar but distinct [14]. They tolerate only small amino acids such as Gly and Ala in subsite P1 and prefer hydrophobic, aliphatic residues in subsite P1′.
What is the difference between MMP9 and MMP7?
MMP7 has a shallow hydrophobic substrate-binding pocket. In contrast to MMP9 which has the longest hinge, MMP7 lacks hemopexin and does not have a hinge. Instead, MMP7 contains a variable C-terminal hemopexin-like domain facilitates substrate specificity. The protein of MMP7 is secreted as zymogen.
How are the catalytic domains of MMPs different?
X-ray crystallography has shown that the catalytic domains of the different MMPs have similar structure, but the topology of the active site clefts differs, accounting for some of the differences in substrate specificities.
How is MMP7 used in the treatment of cancer?
MMP7 cleaves collagen III/IV/V/IX/X/XI and proteoglycan indicating that MMP inhibitors can potentially be used in therapies that involved in inhibition tissue degradation, remodeling, anti-angiogenesis and inhibition of tumor invasion.
